Recombinant Human HDAC4 protein

**Background of HDAC4 Recombinant Protein**

Histone deacetylase 4 (HDAC4) is a member of the class IIa HDAC family, which regulates gene expression by modifying chromatin structure through the removal of acetyl groups from histone lysine residues. Unlike class I HDACs, class IIa HDACs (HDAC4. 5. 7. 9) exhibit tissue-specific expression and shuttle between the nucleus and cytoplasm, acting as transcriptional repressors in coordination with co-regulatory complexes. HDAC4 is highly expressed in tissues such as heart, skeletal muscle, and brain, playing critical roles in development, differentiation, and cellular stress responses.

Structurally, HDAC4 contains an N-terminal regulatory domain that mediates protein-protein interactions and a C-terminal catalytic domain. However, its deacetylase activity is intrinsically weak, requiring interaction with corepressors like HDAC3 for full functionality. HDAC4 primarily regulates non-histone substrates, influencing pathways such as MEF2-mediated transcription, muscle atrophy, and neuronal survival. Dysregulation of HDAC4 is linked to diseases including cancers, neurodegenerative disorders, and cardiovascular conditions, making it a therapeutic target.

Recombinant HDAC4 protein is produced in heterologous systems (e.g., *E. coli* or mammalian cells*) to study its biochemical properties, enzymatic activity, and interactions. Purified HDAC4 is often fused with tags (e.g., GST, His) for efficient isolation and detection. It serves as a vital tool for *in vitro* assays, inhibitor screening, and structural studies to elucidate mechanisms of deacetylation and develop targeted therapies. Research using recombinant HDAC4 has advanced understanding of epigenetic regulation and its role in disease pathogenesis, highlighting its potential in drug discovery and molecular biology.